BMRB Entry 50086

Name: 1H, 15N, 13Ca, 13Cb assignments for yeast Gal4 AD residues 828-881
Published: 2021-03-11

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50086

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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

1H, 15N, 13Ca, 13Cb assignments for yeast Gal4 AD residues 828-881

Deposition date:

2019-11-12

Original release date:

2021-03-11

Authors:

Tuttle, Lisa

Citation:

Citation: Tuttle, Lisa; Pacheco, Derek; Warfield, Linda; Wilburn, Damien; Hahn, Steven; Klevit, Rachel. "Mediator subunit Med15 dictates the conserved fuzzy binding mechanism of yeast transcription activators Gal4 and Gcn4" Nat. Commun. 12, 2220-2220 (2021).
PubMed: 33850123

Assembly members:

Assembly members:
entity_1, polymer, 54 residues, Formula weight is not available

Natural source:

Natural source: Common Name: baker's yeast Taxonomy ID: 4932 Superkingdom: Eukaryota Kingdom: Fungi Genus/species: Saccharomyces cerevisiae

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: SHY823

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: DDGNNSKPLSPGWTDQTAYN AFGITTGMFNTTTMDDVYNY LFDDEDTPPNPKKE

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	142
15N chemical shifts	46
1H chemical shifts	44

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Gal4 AD	1

Entities:

Entity 1, Gal4 AD 54 residues - Formula weight is not available

1

ASP

GLY

ASN

SER

LYS

PRO

LEU

SER

2

PRO

GLY

TRP

THR

ASP

GLN

THR

ALA

TYR

ASN

3

ALA

PHE

GLY

ILE

THR

GLY

MET

PHE

ASN

4

THR

MET

ASP

VAL

TYR

ASN

TYR

5

LEU

PHE

ASP

GLU

ASP

THR

PRO

ASN

6

PRO

LYS

GLU

Samples:

sample_1: sodium phosphate 20 mM; sodium chloride 150 mM; EDTA 0.1 mM; PMSF 0.1 mM; DTT 5 mM; yeast Gal4 AD, [U-100% 13C; U-100% 15N], 560 uM

sample_conditions_1: ionic strength: 150 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMRView, Johnson, One Moon Scientific - chemical shift assignment

NMR spectrometers:

Bruker Avance II 600 MHz MHz

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks